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New page: left|200px<br /> <applet load="1zxm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zxm, resolution 1.87Å" /> '''Human Topo IIa ATPa...
 
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[[Image:1zxm.gif|left|200px]]<br />
<applet load="1zxm" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1zxm, resolution 1.87&Aring;" />
'''Human Topo IIa ATPase/AMP-PNP'''<br />


==Overview==
==Human Topo IIa ATPase/AMP-PNP==
Type IIA DNA topoisomerases play multiple essential roles in the, management of higher-order DNA structure, including modulation of, topological state, chromosome segregation, and chromatin condensation., These diverse physiologic functions are all accomplished through a common, molecular mechanism, wherein the protein catalyzes transient cleavage of a, DNA duplex (the G-segment) to yield a double-stranded gap through which, another duplex (the T-segment) is passed. The overall process is, orchestrated by the opening and closing of molecular "gates" in the, topoisomerase structure, which is regulated by ATP binding, hydrolysis, and release of ADP and inorganic phosphate. Here we present two crystal, structures of the ATPase domain of human DNA topoisomerase IIalpha in, different nucleotide-bound states. Comparison of these structures revealed, rigid-body movement of the structural modules within the ATPase domain, suggestive of the motions of a molecular gate.
<StructureSection load='1zxm' size='340' side='right'caption='[[1zxm]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1zxm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZXM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZXM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.87&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zxm OCA], [https://pdbe.org/1zxm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zxm RCSB], [https://www.ebi.ac.uk/pdbsum/1zxm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zxm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TOP2A_HUMAN TOP2A_HUMAN] Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Essential during mitosis and meiosis for proper segregation of daughter chromosomes.<ref>PMID:22323612</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zx/1zxm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zxm ConSurf].
<div style="clear:both"></div>


==Disease==
==See Also==
Known diseases associated with this structure: DNA topoisomerase II, resistance to inhibition of, by amsacrine OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=126430 126430]]
*[[Topoisomerase 3D structures|Topoisomerase 3D structures]]
 
== References ==
==About this Structure==
<references/>
1ZXM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and ANP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA_topoisomerase_(ATP-hydrolyzing) DNA topoisomerase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.99.1.3 5.99.1.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZXM OCA].
__TOC__
 
</StructureSection>
==Reference==
Nucleotide-dependent domain movement in the ATPase domain of a human type IIA DNA topoisomerase., Wei H, Ruthenburg AJ, Bechis SK, Verdine GL, J Biol Chem. 2005 Nov 4;280(44):37041-7. Epub 2005 Aug 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16100112 16100112]
[[Category: DNA topoisomerase (ATP-hydrolyzing)]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bechis, S.K.]]
[[Category: Bechis SK]]
[[Category: Ruthenburg, A.J.]]
[[Category: Ruthenburg AJ]]
[[Category: Verdine, G.L.]]
[[Category: Verdine GL]]
[[Category: Wei, H.]]
[[Category: Wei H]]
[[Category: ANP]]
[[Category: MG]]
[[Category: ghkl nucleotide-binding fold]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:42:51 2007''

Latest revision as of 09:07, 14 February 2024

Human Topo IIa ATPase/AMP-PNP

1zxm, resolution 1.87Å

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